 |
PDBsum entry 2x86
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
The crystal structure of the y140f mutant of ADP-L-Glycero-D-Manno-Heptose 6-Epimerase bound to ADP-Beta-D-Mannose suggests a one base mechanism.
|
|
|
Authors
|
|
T.Kowatz,
J.P.Morrison,
M.E.Tanner,
J.H.Naismith.
|
|
|
Ref.
|
|
Protein Sci, 2010,
19,
1337-1343.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
Bacteria synthesize a wide array of unusual carbohydrate molecules, which they
use in a variety of ways. The carbohydrate L-glycero-D-manno-heptose is an
important component of lipopolysaccharide and is synthesized in a complex series
of enzymatic steps. One step involves the epimerization at the C6'' position
converting ADP-D-glycero-D-manno-heptose into ADP-L-glycero-D-manno-heptose. The
enzyme responsible is a member of the short chain dehydrogenase superfamily,
known as ADP-L-glycero-D-manno-heptose 6-epimerase (AGME). The structure of the
enzyme was known but the arrangement of the catalytic site with respect to the
substrate is unclear. We now report the structure of AGME bound to a substrate
mimic, ADP-beta-D-mannose, which has the same stereochemical configuration as
the substrate. The complex identifies the key residues and allows mechanistic
insight into this novel enzyme.
|
|
|
|
|
|
|
